Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis.

The Biochemical journal - 1 Sept 2007

Vararattanavech Ardcharaporn, Ketterman Albert J

Abstract excerpt

The present study characterized conserved residues in a GST (glutathione transferase) in the active-site region that interacts with glutathione. This region of the active site is near the glycine moiety of glutathione and consists of a hydrogen bond network. In the GSTD (Delta class GST) studied, adGSTD4-4, the network consisted of His(38), Met(39), Asn(47), Gln(49), His(50) and Cys(51). In addition to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Enzyme Stability
Share to Glutathione

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glutathione Transferase

Share to Glycine

Share to Hydrogen Bonding

Share to Hydrogen-Ion Concentration

Share to Viscosity

Source

Open in PubMed Open full text

Identifiers

PMID: 17523921
DOI: 10.1042/BJ20070422
PMCID: PMC1948969

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis.PMID 17523921Read ↗

Glutamate-64, a newly identified residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferases.Semantic proximity Read ↗

Human glutathione transferase T2-2 discloses some evolutionary strategies for optimization of substrate binding to the active site of glutathione transferases.Semantic proximity Read ↗

Function of conserved residues of human glutathione synthetase: implications for the ATP-grasp enzymes.Semantic proximity Read ↗

Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1.Semantic proximity Read ↗

Identification and clarification of the role of key active site residues in bacterial glutathione S-transferase zeta/maleylpyruvate isomerase.Semantic proximity Read ↗

The structural roles of a conserved small hydrophobic core in the active site and an ionic bridge in domain I of Delta class glutathione S-transferase.Semantic proximity Read ↗

Effects of conserved Arg20, Glu74 and Asp77 on the structure and function of a tau class glutathione S-transferase in rice.Semantic proximity Read ↗

The role of the glycine triad in human glutathione synthetase.Semantic proximity Read ↗

Glutathione transferase A1-1: catalytic importance of arginine 15.Semantic proximity Read ↗

The catalytic site of glutathione peroxidases.Semantic proximity Read ↗

Structural basis for evolution of product diversity in soybean glutathione biosynthesis.Semantic proximity Read ↗

The Multifaceted Role of Glutathione S-Transferases in Health and DiseaseSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.